| 货号 | MTM100 |
| 描述 | The Quantikine Mouse TIMP-1 Immunoassay is a 4.5 hour solid-phase ELISA designed to measure mouse TIMP-1 in cell culture supernates, serum, and plasma. It contains NS0-expressed recombinant mouse TIMP-1 and antibodies raised against the recombinant factor. This immunoassay has been shown to accurately quantitate the recombinant factor. Results obtained using natural mouse TIMP-1 showed linear curves that were parallel to the standard curves obtained using the Quantikine kit standards. These results indicate that this kit can be used to determine relative levels of natural mouse TIMP-1. |
| 别名 | CLGI; Collagenase inhibitor; collagenase inhibitor); EPATIMP-1; EPO; erythroid potentiating activity; Erythroid-potentiating activity; Fibroblast collagenase inhibitor; FLJ90373; HCI; metalloproteinase inhibitor 1; TIMP metallopeptidase inhibitor 1; TIMPtissue inhibitor of metalloproteinase 1 (erythroid potentiating activity; Tissue inhibitor of metalloproteinases 1; | 全称 | Tissue Inhibitors of Metalloproteinases 1 |
| 反应种属 | Mouse |
| 目标/特异性 | Natural and recombinant mouse TIMP-1. This kit detects approximately 80% of the recombinant mouse TIMP-1 complexed with the pro-form of recombinant mouse MMP-9 and approximately 60% when complexed with active recombinant mouse MMP-9. |
| 供应商 | R&D Systems |
| 检测类型 | Solid Phase Sandwich ELISA |
| Entrez Gene IDs | 7076 (Human); 21857 (Mouse); 116510 (Rat) |
| 应用文献 | |
| R&D Systems personnel manually curate a database that contains references using R&D Systems products. The data collected includes not only links to publications in PubMed, but also provides information about sample types, species, and experimental conditions. Effects of a high-fat diet on spontaneous metastasis of Lewis lung carcinoma in plasminogen activator inhibitor-1 deficient and wild-type mice. | |
| 生物活性 | < 0.5% cross-reactivity observed with available related molecules.< 50% cross-species reactivity observed with species tested. |
| 背景 | TIMPs-1 through -4 regulate the activity of zinc metalloproteases known as MMPs, ADAMs and ADAMTSs. Structurally, TIMPs contain two domains. The N-terminal domain binds to the active site of mature metalloproteases via a 1:1 non-covalent interaction, blocking access of substrates to the catalytic site. In addition, The C-terminal domain of TIMP-1 and TIMP-2 binds to the hemopexin- like domain of pro-MMP-9 and pro-MMP-2, respectively. The latter binding is essential for the cell surface activation of MMP-2 by MMP-14. |
| 运输条件 | Blue Ice |
| 存放说明 | 4℃ |
| 参考文献 |
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